ID R0LY21_ANAPL Unreviewed; 1338 AA.
AC R0LY21;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN ORFNames=Anapl_08388 {ECO:0000313|EMBL:EOB05358.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOB05358.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; KB742696; EOB05358.1; -; Genomic_DNA.
DR Proteomes; UP000296049; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:InterPro.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR CDD; cd20875; C1_ROCK2; 1.
DR CDD; cd11638; HR1_ROCK2; 1.
DR CDD; cd01242; PH_ROCK; 1.
DR CDD; cd22250; ROCK_SBD; 1.
DR CDD; cd05596; STKc_ROCK; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.20.5.730; Single helix bin; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020684; ROCK1/ROCK2.
DR InterPro; IPR037311; ROCK2_HR1.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF28; RHO-ASSOCIATED PROTEIN KINASE 2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR PIRSF; PIRSF037568; Rho_kinase; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF103652; G protein-binding domain; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS51859; RHO_BD; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01207}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EOB05358.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000296049};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 48..310
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 313..381
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 450..526
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 930..998
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 1101..1300
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1211..1266
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 462..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 592..977
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1007..1052
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 503..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037568-1"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR037568-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOB05358.1"
FT NON_TER 1338
FT /evidence="ECO:0000313|EMBL:EOB05358.1"
SQ SEQUENCE 1338 AA; 155894 MW; 91CAAE93493E5B74 CRC64;
SFQDGLNSLV LDLDYPALRK NKNIDNFLNR YEKIVEKIRA LQMKAEDYDV VKVIGRGAFG
EVQLVRHKMT QKVYAMKLLS KFEMIKRSDS AFFWEERDIM AFANSPWVVQ LFCAFQDDKY
LYMVMEYMPG GDLVNLMSNY DVPEKWAKFY TAEVVLALDA IHSMGLIHRD VKPDNMLLDK
YGHLKLADFG TCMKMDETGM VRCDTAVGTP DYISPEVLKS QGGDGYYGRE CDWWSVGVFL
FEMLVGDTPF YADSLVGTYS KIMDHKNSLH FPDDVEISKH AKNLICAFLT DRDVRLGRNG
VEEIKHHPFF KSDQWNWDNI RETAAPVVPE LSSDIDSSNF DDIEDDKGDV ETFPIPKAFV
GNQLPFIGFT YYRDNLLLSD SSQSCRENES VQSSKNEFQK KISKLEEQLS NELQAKDELE
QKYRSTNTRL EKIVKELDEE ITSRKNVESA VRQLEREKAL LQHKNTEYQR KAEHEADKKR
NLENEVNSLK DQLEDLKKRN QNSQISNEKI NQLQRQASNS LLRSESDTAT RLRKNQTEST
KQIQQLEANN RELQDKNCLL ENAKLKLEKD FLNLQSALES ERRDRSHGSE IISDLQGRIS
SLEEEVKNGK SALAKLEMEK RQLQEKLTDL EKEKSNMEID MTYKFKVMQQ NLEQEEAEHK
ATKARLADKN KIYESIEEAK SEAMKEMEKK LLEERALKQK VENRLLEAEK QRSMLDCDLK
QSQQKINELL RQKDILNEDV KNLTLKIEQE TQKRCLTQND LKMQTQQVNT LKMSEKQLKQ
ENNHLQEIKL SLEKQNNELR KERQDADGQM KELQDQLEAE QYFSTLYKTQ VRELKEECEE
KTKLCKEIQQ KIQELQDERD SLAAQLEITL TKADSEQLAR SIAEEQYSDL EKEKIMKELE
IKEMMARHKQ ELTEKDATIA SLEEANRTLT SDVANLANEK EELNNKLKEV QEQITKLKEE
EANIGNIKAQ YEKQLLNERT LKTQAVNKLA EIMNRKGPVK RGADTDVRRK EKENRKLHME
LKSEREKLTQ MMIKYQKEIN EMQAQIAEES QIRIELQMTL DSKDSDIEQL RSQLQSLHIG
LDNSSIGSGP GDTETDDGFP ESRLEGWLSL PVRNNTKKFG WVKKYVIVSS KKILFYDSEQ
DKEQSNPYMV LDIDKLFHVR PVTQTDVYRA DAKEIPRIFQ ILYANEGESK KEQEFPVEPM
GEKSNYICHK GHEFIPTLYH FPTNCEACMK PLWHMFKPPP ALECRRCHIK CHKDHMDKKE
EIIAPCKVYY DISTAKNLLL LANSTEEQQK WVSRLVKKIP KKPPAPDPFA RSSPRTSMKV
QPNQSIRRPS RQLPPNKP
//